Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA. Determined by X-ray diffraction at 2.7 Å resolution. Released 8 Aug 2006.
Explore 2AS5 in 3D Show helices and sheets RCSB PDB PDBe
2AS5 contains 22 α-helices and 62 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 509-517 | 9 | |
| β-strand | 525 | 1 | 17 |
| α-helix | 527-537 | 11 | |
| α-helix | 539-541 | 3 | |
| α-helix | 545-558 | 14 | |
| β-strand | 562-567 | 6 | 17 |
| β-strand | 570-575 | 6 | 17 |
| α-helix | 577-580 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 404-405 | 2 | 10 |
| β-strand | 408-409 | 2 | 10 |
| β-strand | 419 | 1 | 11 |
| β-strand | 423-424 | 2 | 12 |
| β-strand | 432 | 1 | 12 |
| β-strand | 443-444 | 2 | 13 |
| β-strand | 454-462 | 9 | 11 |
| β-strand | 470 | 1 | 11 |
| β-strand | 474-478 | 5 | 12 |
| β-strand | 489-493 | 5 | 14 |
| β-strand | 496-500 | 5 | 14 |
| β-strand | 501-503 | 3 | 11 |
| α-helix | 505-507 | 3 | |
| β-strand | 510-511 | 2 | 13 |
| β-strand | 516-520 | 5 | 12 |
| α-helix | 521-522 | 2 | |
| α-helix | 523-527 | 5 | |
| β-strand | 541-552 | 12 | 11 |
| β-strand | 556-568 | 13 | 11 |
| α-helix | 572-574 | 3 | |
| β-strand | 579-583 | 5 | 15 |
| β-strand | 587-589 | 3 | 16 |
| β-strand | 595-601 | 7 | 15 |
| β-strand | 608-614 | 7 | 16 |
| β-strand | 620-624 | 5 | 16 |
| β-strand | 627-628 | 2 | 15 |
| β-strand | 637-641 | 5 | 15 |
| β-strand | 654-661 | 8 | 16 |
| β-strand | 667 | 1 | 16 |
| α-helix | 669-670 | 2 | |
| β-strand | 671-676 | 6 | 16 |
| α-helix | 677 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 404-405 | 2 | 1 |
| β-strand | 408-409 | 2 | 1 |
| β-strand | 411 | 1 | 2 |
| β-strand | 419 | 1 | 3 |
| β-strand | 423-424 | 2 | 4 |
| β-strand | 432 | 1 | 4 |
| β-strand | 443-444 | 2 | 2 |
| β-strand | 454-462 | 9 | 3 |
| β-strand | 470 | 1 | 3 |
| β-strand | 474-478 | 5 | 4 |
| β-strand | 489-490 | 2 | 5 |
| β-strand | 493 | 1 | 6 |
| β-strand | 496 | 1 | 6 |
| β-strand | 499-500 | 2 | 5 |
| β-strand | 501-503 | 3 | 3 |
| α-helix | 505-507 | 3 | |
| β-strand | 510-511 | 2 | 2 |
| β-strand | 516-520 | 5 | 4 |
| α-helix | 523-527 | 5 | |
| β-strand | 541-552 | 12 | 3 |
| β-strand | 556-568 | 13 | 3 |
| α-helix | 572-575 | 4 | |
| β-strand | 579-583 | 5 | 7 |
| β-strand | 587-589 | 3 | 8 |
| β-strand | 595-601 | 7 | 7 |
| β-strand | 608-614 | 7 | 9 |
| β-strand | 620-624 | 5 | 9 |
| β-strand | 627-628 | 2 | 7 |
| β-strand | 637-641 | 5 | 7 |
| α-helix | 643-645 | 3 | |
| β-strand | 656-661 | 6 | 9 |
| β-strand | 667 | 1 | 9 |
| α-helix | 669-670 | 2 | |
| β-strand | 671-673 | 3 | 9 |
| β-strand | 674-676 | 3 | 8 |
| α-helix | 677 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5'-d(tp*tp*ap*gp*gp*ap*ap*ap*ap*tp*tp*tp*gp*tp*tp*tp*cp*ap*tp*ap*gp*)-3' | A, C | DNA | 21 | ||
| 5'-d(ap*ap*cp*tp*ap*tp*gp*ap*ap*ap*cp*ap*ap*ap*tp*tp*tp*tp*cp*cp*tp*)-3' | B, D | DNA | 21 | ||
| Nuclear factor of activated T-cells, cytoplasmic 2 | M, N | protein | 287 | Homo sapiens | Q13469 (AlphaFold model) |
| Forkhead box protein P2 | F, G | protein | 93 | Homo sapiens | O15409 (AlphaFold model) |
>2AS5_1 5'-D(TP*TP*AP*GP*GP*AP*AP*AP*AP*TP*TP*TP*GP*TP*TP*TP*CP*AP*TP*AP*GP*)-3' (chains A, C) TTAGGAAAATTTGTTTCATAG
>2AS5_2 5'-D(AP*AP*CP*TP*AP*TP*GP*AP*AP*AP*CP*AP*AP*AP*TP*TP*TP*TP*CP*CP*TP*)-3' (chains B, D) AACTATGAAACAAATTTTCCT
>2AS5_3 Nuclear factor of activated T-cells, cytoplasmic 2 (chains M, N) ASLPPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMEN KPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRA TIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQTASNPIECSQ RSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKD KSQPNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPV
>2AS5_4 Forkhead box protein P2 (chains F, G) IVRPPFTYATLIRQAIMESSDRQLTLNEIYSWFTRTFAYFRRNAATWKNAVRHNLSLHKC FVRVENVKGAVWTVDEVEYQKRRSQKITGSPTL
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
FOXP3 Controls Regulatory T Cell Function through Cooperation with NFAT. Wu, Y., Borde, M., Heissmeyer, V. et al. Cell (2006) 126:375-387. DOI 10.1016/j.cell.2006.05.042 · PubMed
Other PDB entries of the same protein (UniProt Q13469 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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